Templated Collagen “Double Helices” Maintain Their Structure
Name
nihms-1067138.pdf
Description
Accepted version
Size
1.26 MB
Format
Unknown
Checksum (MD5)
d8e5d9652be95d5b587739cf59a19efe
Author(s)
Tanrikulu, Ismet Caglar
Westler, William M
Ellison, Aubrey J
Markley, John L
Raines, Ronald T
Date Issued
2020
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Version
Author's final manuscript
Abstract
© 2020 American Chemical Society. The self-assembly of collagen-mimetic peptides (CMPs) that form sticky-ended triple helices has allowed the production of surprisingly stable artificial collagen fibers and hydrogels. Assembly through sticky ends requires the recognition of a single strand by a templated strand dimer. Although CMPs and their triple helices have been studied extensively, the structure of a strand dimer is unknown. Here, we evaluate the physical characteristics of such dimers, using disulfide-templated (PPG)10 dimers as a model. Such "linked-dimers" retain their collagen-like structure even in the absence of a third strand, but only when their strands are capable of adopting a triple-helical fold. The intrinsic collagen-like structure of templated CMP pairs helps to explain the success of sticky-ended CMP association and changes the conception of new synthetic collagen designs.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1021/JACS.9B07583
